I have a thioredoxin tag with my therapeutic protein. I have purified it using Ni-NTA. Next, I want to check it's activity by Elisa or cell proliferation assay. Is it necessary to remove the tag from the fusion construct in order to carry out bioassay?
The efficient removal of a N- or C-terminal purification tag from a fusion protein is necessary to obtain a protein in a pure and active form, ready for use in human or animal medicine. https://pubmed.ncbi.nlm.nih.gov/9885186/
Check https://www.biopharminternational.com/view/fusion-tags-protein-expression-and-purification
Check this paper.
Article Current affinity approaches for purification of recombinant proteins
Thank you Chinaza Godswill Awuchi and Kiprotich Kiptum I will go through the papers.
Hi Dr Snehal D. Ganjave.Ph.D . Yes. Genetically engineered fusion tags allow the purification of virtually any protein without any prior knowledge of its biochemical properties. They can improve the variable yield and poor solubility of many recombinant proteins. ... For this reason, it is desirable to remove the tag from the target protein after expression. See the link: https://www.biopharminternational.com/view/fusion-tags-protein-expression-and-purification
See the following link: https://www.abcam.com/content/his-tag-protein-production-and-purification
Also see the following RG link: Article Going native: Complete removal of protein purification affin...
kindly see also the following link: https://www.biopharminternational.com/view/fusion-tags-protein-expression-and-purification
Moreover kindly see the following link: https://pef.facility.uq.edu.au/fusion-tags-protein-purification